Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
Generation of Straight or Branched Actin Filaments01:14

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Pathological TDP-43 filaments accumulate at synapses and cause synaptic dysfunction.

bioRxiv : the preprint server for biology·2026
Same author

Synapse-specific and plasticity-regulated AMPA receptor mobility tunes synaptic integration.

Neuron·2026
Same author

Structure and organization of AMPA receptor-TARP complexes in the mammalian cerebellum.

Science (New York, N.Y.)·2025
Same author

'Mini analysis' misrepresents changes in synaptic properties due to incomplete event detection.

The Journal of physiology·2025
Same author

Architecture, dynamics and biogenesis of GluA3 AMPA glutamate receptors.

Nature·2025
Same author

Dopamine increases protein synthesis in hippocampal neurons enabling dopamine-dependent LTP.

eLife·2025

Related Experiment Video

Updated: May 24, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

AMPA receptor assembly: atomic determinants and built-in modulators.

Madhav Sukumaran1, Andrew C Penn, Ingo H Greger

  • 1Laboratory of Cellular and Synaptic MRC LMB and Neurophysiology, National Institutes of Health, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, MD 20892, USA.

Advances in Experimental Medicine and Biology
|February 22, 2012
PubMed
Summary

Glutamate-gated ion channels (iGluRs) form heterotetramers that control brain excitation. Recent structural and RNA processing insights reveal how iGluR subunit assembly shapes neuronal signaling and function.

More Related Videos

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
07:03

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions

Published on: December 23, 2022

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Related Experiment Videos

Last Updated: May 24, 2026

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
11:33

Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking

Published on: December 17, 2013

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions
07:03

Pulldown Assay Coupled with Co-Expression in Bacteria Cells as a Time-Efficient Tool for Testing Challenging Protein-Protein Interactions

Published on: December 23, 2022

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Glutamate-gated ion channels (iGluRs) are crucial for excitatory neurotransmission at glutamatergic synapses.
  • Receptor subunit composition dictates synaptic targeting and signaling properties, influencing neuronal computations.
  • iGluRs assemble as obligatory or preferential heteromers, but the mechanisms remain largely unknown.

Purpose of the Study:

  • To review recent advances in understanding iGluR assembly mechanisms.
  • To highlight the role of atomic determinants in assembly domains and RNA processing.
  • To discuss the physiological significance of distinct iGluR heterotetramers in modulating neurotransmission.

Main Methods:

  • Review of recent structural biology studies on iGluRs.
  • Analysis of atomic determinants in iGluR assembly domains.
  • Examination of alternative RNA processing in the ligand-binding domain.

Main Results:

  • Recent structural data illuminate atomic determinants governing iGluR heteromeric assembly.
  • Alternative RNA processing in the ligand-binding domain influences subunit interfaces and receptor formation.
  • Distinct iGluR heterotetramers exhibit unique physiological roles in modulating excitatory neurotransmission.

Conclusions:

  • Understanding iGluR assembly is key to deciphering neuronal function.
  • Modulation of iGluR formation via RNA processing offers a regulatory mechanism.
  • Targeting specific iGluR heterotetramers may hold therapeutic potential for neurological disorders.